Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1372320 | Bioorganic & Medicinal Chemistry Letters | 2013 | 4 Pages |
Abstract
STAT3 (Signal Transducer and Activator of Transcription factor 3) is constitutively active in a wide range of human tumours. Stattic is one of the first non-peptidic small molecules reported to inhibit formation of the STAT3:STAT3 protein dimer complex. A mass spectrometry method has been developed to investigate the binding of Stattic to the un-phosphorylated STAT3βtc (U-STAT3) protein. Alkylation of four cysteine residues has been observed with possible reaction at a fifth which could account for the mechanism of action.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Sibylle Heidelberger, Giovanna Zinzalla, Dyeison Antonow, Samantha Essex, B. Piku Basu, Jonathan Palmer, Jarmila Husby, Paul J.M. Jackson, Khondaker M. Rahman, Andrew F. Wilderspin, Mire Zloh, David E. Thurston,